The long term survival of bacteria in both environmental and medical settings depends on their ability to survive the stress associated with periods of nutrient limitation. During these periods, reaction byproducts accumulate to near lethal levels. Many bacteria overcome this stress by synthesizing proteins whose sole purpose is to detoxify the environment by scavenging free radicals. Understanding how bacteria avoid stress-induced death has far reaching consequences for the development of anti-bacterial agents. Blue Copper Protein (BCP) is synthesized in the late stationary phase in Thiosphaera pantotropha, to levels of 20% or more of the total periplasmic protein. BCP is categorized as a monooyxgenase, and has been shown to reduce oxygen with periplasmic transfer proteins as electron donors. We therefore seek time to determine the structure of BCP by a combination of MAD and MIR techniques.